ArticleProceedings of the National Academy of Sciences of the United States of America2008
Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 136 citations in OpenAlex.
- Article
- YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026Article
- The gram-positive HtrA, the protease that is also a chaperone.Journal of bacteriology · 2026Review
- Streptococcus pneumoniae HtrA is a dynamic and monomeric virulence factor capable of forming larger oligomeric complexes.Protein science : a publication of the Protein Society · 2026Article
- Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- HtrA, fatty acids, and membrane protein interplay inJournal of bacteriology · 2024Article
- HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species.Nature communications · 2024Article
- σMolecular microbiology · 2021Article
- Computational Design of Novel Allosteric Inhibitors forMolecules (Basel, Switzerland) · 2021Article
- Identification and Characterization of Plasmin-Independent Thrombolytic Enzymes.Circulation research · 2021Article
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Functional analysis and cryo-electron microscopy ofGut microbes · 2020Article
- Roles of the Site 2 Protease Eep in Staphylococcus aureus.Journal of bacteriology · 2020Article
- Activation by substoichiometric inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The serine protease HtrA1 cleaves misfolded transforming growth factor β-induced protein (TGFBIp) and induces amyloid formation.The Journal of biological chemistry · 2019Article
- The Role of Proteases in the Virulence of Plant Pathogenic Bacteria.International journal of molecular sciences · 2019Review
11 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Aberrant proteins represent an extreme hazard to cells. Therefore, molecular chaperones and proteases have to carry out protein quality control in each cellular compartment. In contrast to the ATP-dependent cytosolic proteases and chaperones, the molecular mechanisms of extracytosolic factors are largely unknown. To address this question, we studied the protease function of DegP, the central housekeeping protein in the bacterial envelope. Our data reveal that DegP processively degrades misfolded proteins into peptides of defined size by employing a molecular ruler comprised of the PDZ1 domain and the proteolytic site. Furthermore, peptide binding to the PDZ domain transforms the resting protease into its active state. This allosteric activation mechanism ensures the regulated and rapid elimination of misfolded proteins upon folding stress. In comparison to the cytosolic proteases, the regulatory features of DegP are established by entirely different mechanisms reflecting the convergent evolution of an extracytosolic housekeeping protease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.